Abstract:
:Deletion of elongation factor-like 1 (Efl1p), a cytoplasmic GTPase homologous to the ribosomal translocases EF-G/EF-2, results in nucle(ol)ar pre-rRNA processing and pre-60S subunits export defects. Efl1p interacts genetically with Tif6p, a nucle(ol)ar protein stably associated with pre-60S subunits and required for their synthesis and nuclear exit. In the absence of Efl1p, 50% of Tif6p is relocated to the cytoplasm. In vitro, the GTPase activity of Efl1p is stimulated by 60S, and Efl1p promotes the dissociation of Tif6p-60S complexes. We propose that Tif6p binds to the pre-60S subunits in the nucle(ol)us and escorts them to the cytoplasm where the GTPase activity of Efl1p triggers a late structural rearrangement, which facilitates the release of Tif6p and its recycling to the nucle(ol)us.
journal_name
Mol Celljournal_title
Molecular cellauthors
Senger B,Lafontaine DL,Graindorge JS,Gadal O,Camasses A,Sanni A,Garnier JM,Breitenbach M,Hurt E,Fasiolo Fdoi
10.1016/s1097-2765(01)00403-8subject
Has Abstractpub_date
2001-12-01 00:00:00pages
1363-73issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00403-8journal_volume
8pub_type
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